ID   TCPD_DICDI              Reviewed;         533 AA.
AC   Q54CL2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=cct4; ORFNames=DDB_G0292872;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins upon ATP
CC       hydrolysis. Known to play a role, in vitro, in the folding of actin and
CC       tubulin (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that forms
CC       two stacked rings, 12 to 16 nm in diameter. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR   EMBL; AAFI02000197; EAL60985.1; -; Genomic_DNA.
DR   RefSeq; XP_629404.1; XM_629402.1.
DR   AlphaFoldDB; Q54CL2; -.
DR   SMR; Q54CL2; -.
DR   STRING; 44689.DDB0233993; -.
DR   PaxDb; Q54CL2; -.
DR   EnsemblProtists; EAL60985; EAL60985; DDB_G0292872.
DR   GeneID; 8628923; -.
DR   KEGG; ddi:DDB_G0292872; -.
DR   dictyBase; DDB_G0292872; cct4.
DR   eggNOG; KOG0358; Eukaryota.
DR   HOGENOM; CLU_008891_9_1_1; -.
DR   InParanoid; Q54CL2; -.
DR   OMA; HPAANMI; -.
DR   PhylomeDB; Q54CL2; -.
DR   BRENDA; 3.6.4.B10; 1939.
DR   Reactome; R-DDI-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-DDI-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:Q54CL2; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; ISS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd03338; TCP1_delta; 1.
DR   Gene3D; 1.10.560.10; -; 1.
DR   Gene3D; 3.30.260.10; -; 1.
DR   Gene3D; 3.50.7.10; -; 1.
DR   InterPro; IPR012717; Chap_CCT_delta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR   InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR   InterPro; IPR027413; GROEL-like_equatorial_sf.
DR   InterPro; IPR027410; TCP-1-like_intermed_sf.
DR   PANTHER; PTHR11353; PTHR11353; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; SSF48592; 1.
DR   SUPFAM; SSF52029; SSF52029; 1.
DR   SUPFAM; SSF54849; SSF54849; 1.
DR   TIGRFAMs; TIGR02342; chap_CCT_delta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..533
FT                   /note="T-complex protein 1 subunit delta"
FT                   /id="PRO_0000327382"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   533 AA;  56918 MW;  34101BE3C7918F6B CRC64;
     MSAPAAAPAK VLPSRSDFDE KEKEKDVRTS NIVAARAVAD AIRTSLGPKG MDKMIISPNN
     EVLISNDGAT ILQNLELRHP AAKMLAELAK AQDIEAGDGT TSVCVIAGSL LGAVSQLMAK
     GIHPSIISEA FNLALNKSLE VLVSMSVPVS LTDRVSLVKS ATTSLNSKVV SQYTNLASIA
     VDAVLSVINP ATAVNVNLKD IKLIKKLGGT IEDTELVQGL VFDQTASHTA GGPTRIQNAK
     IGLIQFCLSA PKTYMDNNIV VSDYSKMDKV IKEEPKLILE MCRKIQKSGC NVLLVQKSIL
     RDAVNDLSLH YLAKLKILVI KDIERDDIEF ICNTIGCQPV ANIDSFTADK LGKADLVEEV
     GTSDGKIVKV TGIPNPGKTV TVLCRGSNKL VLDEAERSLH DALCVIRSLV KKKFLIAGGG
     APEIEVSQQV TAFSKTLTGI TSYCVRAYAE ALEIIPYTLA ENAGLHPISI VTELRNKHAQ
     GEINSGINVR KGAITNILQE NVVQPLLVST SALTLATETV VMLLKIDDIA TAR